REPA_SSVN
ID REPA_SSVN Reviewed; 314 AA.
AC Q89822;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Replication-associated protein A;
DE Short=RepA;
DE EC=3.1.21.-;
GN ORFNames=C1;
OS Sugarcane streak virus (isolate South Africa) (SSV) (Sugarcane streak virus
OS (isolate Natal)).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=268781;
OH NCBI_TaxID=173841; Cenchrus echinatus.
OH NCBI_TaxID=4547; Saccharum officinarum (Sugarcane).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hughes F.L.;
RT "Molecular investigations of subgroup 1 geminiviruses.";
RL Thesis (1991), University of Cape Town, South Africa.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8352656; DOI=10.1007/bf01309851;
RA Hughes F.L., Rybicki E.P., Kirby R.;
RT "Complete nucleotide sequence of sugarcane streak Monogeminivirus.";
RL Arch. Virol. 132:171-182(1993).
CC -!- FUNCTION: Implicated in enhancement of V-sense gene expression. Acts a
CC an inhibitor of C-sense gene transcription (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Part of the C- and V-complexes which are RepA-
CC Rep-DNA complexes involved in the c-sense and v-sense transcription (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RepA;
CC IsoId=Q89822-1; Sequence=Displayed;
CC Name=Rep;
CC IsoId=Q80GM6-1; Sequence=External;
CC -!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2 may
CC be involved in metal coordination. RCR-3 is required for phosphodiester
CC bond cleavage for initiation of RCR.
CC -!- DOMAIN: The LXCXE motif specifically binds to host RBR1. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform RepA]: Produced from the unspliced transcript.
CC -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC {ECO:0000305}.
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DR EMBL; M82918; AAA47830.1; -; Genomic_DNA.
DR EMBL; S64567; AAP13957.1; -; Genomic_DNA.
DR SMR; Q89822; -.
DR Proteomes; UP000007230; Genome.
DR Proteomes; UP000204673; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR InterPro; IPR001146; Gemini_AL1_MSV.
DR InterPro; IPR001191; Gemini_AL1_REP.
DR InterPro; IPR022690; Gemini_AL1_REP_cat-dom.
DR InterPro; IPR022692; Gemini_AL1_REP_central.
DR Pfam; PF00799; Gemini_AL1; 1.
DR Pfam; PF08283; Gemini_AL1_M; 1.
DR PRINTS; PR00227; GEMCOATAL1.
DR PRINTS; PR00229; GEMCOATMSVL1.
PE 3: Inferred from homology;
KW Activator; Alternative splicing; DNA-binding; Endonuclease;
KW G1/S host cell cycle checkpoint dysregulation by virus; Host cytoplasm;
KW Host nucleus; Host-virus interaction; Hydrolase; Metal-binding;
KW Modulation of host cell cycle by virus; Nuclease; Reference proteome;
KW Repressor.
FT CHAIN 1..314
FT /note="Replication-associated protein A"
FT /id="PRO_0000316944"
FT REGION 180..192
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 255..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 24..28
FT /note="RCR-1"
FT MOTIF 66..71
FT /note="RCR-2"
FT MOTIF 106..109
FT /note="RCR-3"
FT COMPBIAS 255..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
SQ SEQUENCE 314 AA; 34940 MW; 33854BB4235234F3 CRC64;
MSTVGSTVSS TPSRRFKHRN VNTFLTYSRC PLEPEAVGLH IWSLIAHWTP VYVLSVRETH
EDGGYHIHVL AQSAKPVYTT DSGFFDIDGF HPNIQSAKSA NKVRAYAMKN PVTYWERGTF
IPRKTSFLGD STEPNSKKQS KDDIVRDIIE HSTNKQEYLS MIQKALPYEW ATKLQYFEYS
ANKLFPDIQE IYTSPFPQST PALLDPTAIN TWLENNLYQV SPSAYMLANP SCLTLEEATS
DLIWMHETSR TLIPTGSSAC TSSGQQEQAS PPGPGAWEDI ITGRTTSTGP PTTRTQNTTS
STTYPSSTVH AGSN
